PT  - JOURNAL ARTICLE
AU  - Hurtley, Stella M.
TI  - Peripheral Quality Control
AID  - 10.1126/scisignal.3135ec253
DP  - 2010 Aug 17
TA  - Science Signaling
PG  - ec253--ec253
VI  - 3
IP  - 135
4099  - http://stke.sciencemag.org/content/3/135/ec253.short
4100  - http://stke.sciencemag.org/content/3/135/ec253.full
SO  - Sci. Signal.2010 Aug 17; 3
AB  - Protein misfolding diseases often lead to the retention and degradation of important proteins within the endoplasmic reticulum (ER). Strategies to reduce the stringency of ER quality control that allow the proteins to carry on through the secretory pathway to reach their destination at the cell surface have shown some promise. Okiyoneda et al. (see the Perspective by Hutt and Balch) wanted to understand how, even if a protein reaches its destination, it may still be subjected to a second level of quality control and be cleared from the plasma membrane. Using functional small-interfering RNA screens in cells expressing the common cystic fibrosis mutation F508CFTR, the authors identified a pair of chaperones that promoted clearance of defective proteins from the plasma membrane. This peripheral quality-control step will also need to be overcome to increase the effectiveness of strategies to overcome protein misfolding disorders. T. Okiyoneda, H. Barrière, M. Bagdány, W. M. Rabeh, K. Du, J. Höhfeld, J. C. Young, G. L. Lukacs, Peripheral protein quality control removes unfolded CFTR from the plasma membrane. Science 329, 805–810 (2010). [Abstract] [Full Text] D. Hutt, W. E. Balch, The proteome in balance. Science 329, 766–767 (2010). [Summary] [Full Text]